Publications by authors named "Eckfeld K"
RASSF family proteins are tumor suppressors that are frequently downregulated during the development of human cancer. The best-characterized member of the family is RASSF1A, which is downregulated by promoter methylation in 40-90% of primary human tumors. We now identify and characterize a novel member of the RASSF family, RASSF6.
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- RASSF1A is a tumor suppressor that is often silenced in tumors due to promoter methylation, affecting important cellular functions like cell cycle regulation and apoptosis.
- The study reveals a new pathway where RASSF1A interacts with the protein MOAP-1, which is crucial for activating Bax, a protein that promotes cell death, particularly when K-Ras is activated.
- Tumor-derived mutations in RASSF1A disrupt its interaction with MOAP-1 and impair Bax activation, highlighting a critical pro-apoptotic pathway involving K-Ras, RASSF1A, and Bax that is compromised in some cancers.
Ras proteins are members of a superfamily of related small GTPases. Some members, such as Ras, are oncogenic. However, other members seem to serve as tumor suppressors, such as Rig and Noey2.
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- Activated Ras proteins engage with various effector proteins, leading to different biological outcomes, including both cell growth and growth-inhibitory effects like senescence or apoptosis.
- The RASSF family, known for its role as Ras effector/tumor suppressors, includes four known members, and research has now identified a fifth member, RASSF4, which shares significant genetic similarity with RASSF1A and RASSF2.
- RASSF4 interacts directly with activated K-Ras and promotes apoptosis in certain cells while being frequently down-regulated in human tumors due to promoter methylation, highlighting its potential role as a tumor suppressor.
Junctional adhesion molecule 1 (JAM-1) was the first of a family of related proteins (JAM family) to be discovered. Two proteins with structural and sequence similarities to JAM-1, named JAM-2 and JAM-3, have been identified more recently. JAM-1 is specifically localized at the tight junctions of epithelial and endothelial cells and is involved in the regulation of junctional integrity and permeability.
View Article and Find Full Text PDFWe have previously reported the purification and characterization of a 32 kDa platelet surface glycoprotein that is recognized by the stimulatory monoclonal antibody, F11. The cDNA has been cloned and found to encode the human homolog of the murine junctional adhesion molecule, JAM; we therefore named this human homolog JAM-1. Northern blot analysis indicated that JAM-1 mRNA is expressed as multiple species, the predominant transcript being approximately 4.
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